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Altogether, these data provide new insight into the central role of ACBD3 in recruiting PI4KB by enterovirus 3A and reveal the minimal domains of ACBD3 involved in recruiting PI4KB and supporting enterovirus replication.
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These results reveal a mechanism of EV71 replication that involves host ACBD3 for viral replication.
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that ACBD3 may represent candidate therapeutic targets to enable the elimination of breast cancer stem cells
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ACBD3 was found as a gene expression variability marker in 8-cell human embryos.
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the component proteins of the machinery, OSBP, VAP, SAC1, and PITPNB, are all essential host factors for AiV replication. Importantly, the machinery is directly recruited to the RNA replication sites through previously unknown interactions of VAP/OSBP/SAC1 with the AiV proteins and with ACBD3.
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Results show that Aichi virus 3A protein activates the lipid kinase activity of PI4KIIIb,which activation is sensitized by the protein ACBD3. The interfaces between PI4KIIIbeta-ACBD3 and ACBD3-3A were mapped with hydrogen-deuterium exchange mass spectrometry.
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Kobuviral non-structural 3A proteins act as molecular harnesses to hijack the host ACBD3 protein.
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The authors propose a model in which interaction between Salmonella enterica serovar Typhimurium SseF and SseG enables both proteins to bind ACBD3, thereby anchoring Salmonella-containing vacuoles at the Golgi network and facilitating bacterial replication.
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these findings suggest that ACBD3 has prominent impacts on cellular NAD(+) metabolism via regulating PARP1 activation-dependent auto-modification and thus cell metabolism and function.
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Authors found that NS5A and PI4KB competed for association of acyl-coenzyme A binding domain containing protein 3 (ACBD3), which inhibited hepatitis C virus replication.
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Host ACBD3, PI4KIIIBETA and Aichi virus proteins complexes enhances phosphatidylinositol 4-phosphate synthesis and is critical for viral replication.
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ACBD3 mediates mHtt cytotoxicity via a Rhes/mHtt/ACBD3 complex.
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Authors found that the Golgi protein acyl-coenzyme A binding domain-containing 3 (ACBD3), interacts with the 3A proteins of poliovaccine Sabintpe 2 and coxsackievirus A17 at viral RNA replication sites.
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Using affinity purification-mass spectrometry, we identified the putative Rab33 GTPase-activating proteins TBC1D22A and TBC1D22B as ACBD3-interacting factors.
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ACBD3 plays an essential role in maintaining lipid homeostasis via regulating SREBP1's processing pathway and thus impacting cellular lipogenesis.
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identified ACBD3 as an interacting partner of PPM1L, and showed that this association, which recruits PPM1L to ER-Golgi membrane contact sites, is mediated by a GOLD (Golgi dynamics) domain in ACBD3
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The data were consistent with PAP7 interacting with DMT1 and regulating DMT1 expression in K562 cells by modulating expression of DMT1 protein.
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The 3A protein of picornaviruses utilizes the golgi adaptor protein ACBD3 to recruit PI4KIIIbeta.
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results indicate that a viral protein/ACBD3/PI4KB complex is formed to synthesize PI4P at the AiV RNA replication sites and plays an essential role in viral RNA replication
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Molecular cloning, chromosomal localization and expression pattern of PAP7.
